1SET
CRYSTAL STRUCTURES AT 2.5 ANGSTROMS RESOLUTION OF SERYL-TRNA SYNTHETASE COMPLEXED WITH TWO DIFFERENT ANALOGUES OF SERYL-ADENYLATE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004828 | molecular_function | serine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006434 | biological_process | seryl-tRNA aminoacylation |
| A | 0016260 | biological_process | selenocysteine biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0070905 | molecular_function | serine binding |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004828 | molecular_function | serine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006434 | biological_process | seryl-tRNA aminoacylation |
| B | 0016260 | biological_process | selenocysteine biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0070905 | molecular_function | serine binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE SSA A 422 |
| Chain | Residue |
| A | THR225 |
| A | GLU279 |
| A | GLU345 |
| A | THR346 |
| A | HIS347 |
| A | SER348 |
| A | ASN378 |
| A | THR380 |
| A | ALA383 |
| A | HOH427 |
| A | HOH459 |
| A | GLU227 |
| A | HOH502 |
| A | ARG256 |
| A | GLU258 |
| A | MET270 |
| A | ARG271 |
| A | VAL272 |
| A | PHE275 |
| A | LYS277 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE SSA B 423 |
| Chain | Residue |
| B | THR225 |
| B | GLU227 |
| B | ARG256 |
| B | GLU258 |
| B | MET270 |
| B | ARG271 |
| B | VAL272 |
| B | PHE275 |
| B | GLU279 |
| B | GLU345 |
| B | THR346 |
| B | HIS347 |
| B | SER348 |
| B | ASN378 |
| B | THR380 |
| B | HOH469 |
| B | HOH477 |
| B | HOH478 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU345 | |
| A | THR380 | |
| B | THR225 | |
| B | ARG256 | |
| B | VAL272 | |
| B | GLU279 | |
| B | GLU345 | |
| B | THR380 | |
| A | THR225 | |
| A | ARG256 | |
| A | VAL272 | |
| A | GLU279 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| A | ARG256 | electrostatic stabiliser |
| A | ARG271 | electrostatic stabiliser |
| A | GLU345 | metal ligand |
| A | SER348 | metal ligand |
| A | ARG386 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 884 |
| Chain | Residue | Details |
| B | ARG256 | electrostatic stabiliser |
| B | ARG271 | electrostatic stabiliser |
| B | GLU345 | metal ligand |
| B | SER348 | metal ligand |
| B | ARG386 | electrostatic stabiliser |
